ID   GRIK5_HUMAN             Reviewed;         980 AA.
AC   Q16478; Q8WWG8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   11-NOV-2015, entry version 149.
DE   RecName: Full=Glutamate receptor ionotropic, kainate 5;
DE            Short=GluK5;
DE   AltName: Full=Excitatory amino acid receptor 2;
DE            Short=EAA2;
DE   AltName: Full=Glutamate receptor KA-2;
DE            Short=KA2;
DE   Flags: Precursor;
GN   Name=GRIK5; Synonyms=GRIK2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Hippocampus;
RX   PubMed=1321949;
RA   Kamboj R.K., Schoepp D.D., Nutt S., Shekter L., Korczak B., True R.A.,
RA   Zimmerman D.M., Wosnick M.A.;
RT   "Molecular structure and pharmacological characterization of humEAA2,
RT   a novel human kainate receptor subunit.";
RL   Mol. Pharmacol. 42:10-15(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Erythroleukemia;
RA   Langer A., Xu D., Kuehcke K., Fehse B., Abdallah S., Lother H.;
RT   "Myeloid progenitor cell growth and apoptosis involves known and cell-
RT   specific ionotropic glutamate receptors.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for glutamate. L-glutamate acts as an
CC       excitatory neurotransmitter at many synapses in the central
CC       nervous system. The postsynaptic actions of Glu are mediated by a
CC       variety of receptors that are named according to their selective
CC       agonists. This receptor binds kainate > quisqualate > domoate > L-
CC       glutamate >> AMPA >> NMDA = 1S,3R-ACPD.
CC   -!- SUBUNIT: Tetramer of two or more different subunits. Associates
CC       with GRIK1 (both edited and unedited versions), GRIK2, or GRIK3 to
CC       form functional channels. Homomeric associations do not produce
CC       any channel activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, synapse, postsynaptic cell membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q16478-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q16478-2; Sequence=VSP_035585;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC       (TC 1.A.10.1) family. GRIK5 subfamily. {ECO:0000305}.
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DR   EMBL; S40369; AAB22591.1; -; mRNA.
DR   EMBL; AJ249209; CAC80547.1; -; mRNA.
DR   EMBL; CH471126; EAW57090.1; -; Genomic_DNA.
DR   CCDS; CCDS12595.1; -. [Q16478-1]
DR   CCDS; CCDS77305.1; -. [Q16478-2]
DR   PIR; I57936; I57936.
DR   RefSeq; NP_001287959.1; NM_001301030.1. [Q16478-2]
DR   RefSeq; NP_002079.3; NM_002088.4. [Q16478-1]
DR   RefSeq; XP_005258878.1; XM_005258821.2. [Q16478-1]
DR   RefSeq; XP_011525165.1; XM_011526863.1. [Q16478-2]
DR   UniGene; Hs.367799; -.
DR   ProteinModelPortal; Q16478; -.
DR   SMR; Q16478; 22-828.
DR   BioGrid; 109158; 7.
DR   IntAct; Q16478; 4.
DR   MINT; MINT-1427286; -.
DR   STRING; 9606.ENSP00000262895; -.
DR   BindingDB; Q16478; -.
DR   ChEMBL; CHEMBL2109241; -.
DR   GuidetoPHARMACOLOGY; 454; -.
DR   PhosphoSite; Q16478; -.
DR   BioMuta; GRIK5; -.
DR   DMDM; 209572626; -.
DR   PaxDb; Q16478; -.
DR   PRIDE; Q16478; -.
DR   DNASU; 2901; -.
DR   Ensembl; ENST00000262895; ENSP00000262895; ENSG00000105737. [Q16478-1]
DR   Ensembl; ENST00000301218; ENSP00000301218; ENSG00000105737. [Q16478-2]
DR   Ensembl; ENST00000593562; ENSP00000470251; ENSG00000105737. [Q16478-1]
DR   GeneID; 2901; -.
DR   KEGG; hsa:2901; -.
DR   UCSC; uc002osi.2; human. [Q16478-1]
DR   CTD; 2901; -.
DR   GeneCards; GRIK5; -.
DR   H-InvDB; HIX0022359; -.
DR   H-InvDB; HIX0027521; -.
DR   HGNC; HGNC:4583; GRIK5.
DR   MIM; 600283; gene.
DR   neXtProt; NX_Q16478; -.
DR   PharmGKB; PA28977; -.
DR   eggNOG; ENOG410ISR4; Eukaryota.
DR   eggNOG; ENOG410XRUE; LUCA.
DR   GeneTree; ENSGT00760000118920; -.
DR   HOGENOM; HOG000234371; -.
DR   HOVERGEN; HBG051839; -.
DR   InParanoid; Q16478; -.
DR   KO; K05205; -.
DR   OMA; SANIWSH; -.
DR   OrthoDB; EOG71G9W6; -.
DR   PhylomeDB; Q16478; -.
DR   TreeFam; TF334668; -.
DR   Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor.
DR   GeneWiki; GRIK5; -.
DR   GenomeRNAi; 2901; -.
DR   NextBio; 11483; -.
DR   PRO; PR:Q16478; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; Q16478; -.
DR   CleanEx; HS_GRIK2; -.
DR   CleanEx; HS_GRIK5; -.
DR   ExpressionAtlas; Q16478; baseline and differential.
DR   Genevisible; Q16478; HS.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0032983; C:kainate selective glutamate receptor complex; IBA:GO_Central.
DR   GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR   GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR   GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:UniProtKB.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:GOC.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0006621; P:protein retention in ER lumen; IEA:Ensembl.
DR   GO; GO:0043113; P:receptor clustering; IEA:Ensembl.
DR   GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic membrane; IEA:Ensembl.
DR   GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_rcpt_met.
DR   InterPro; IPR001320; Iontro_rcpt.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell junction; Cell membrane; Complete proteome;
KW   Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Polymorphism;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW   Synapse; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     14       {ECO:0000255}.
FT   CHAIN        15    980       Glutamate receptor ionotropic, kainate 5.
FT                                /FTId=PRO_0000011552.
FT   TOPO_DOM     15    544       Extracellular. {ECO:0000255}.
FT   TRANSMEM    545    565       Helical. {ECO:0000255}.
FT   TOPO_DOM    566    622       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    623    643       Helical. {ECO:0000255}.
FT   TOPO_DOM    644    803       Extracellular. {ECO:0000255}.
FT   TRANSMEM    804    824       Helical. {ECO:0000255}.
FT   TOPO_DOM    825    980       Cytoplasmic. {ECO:0000255}.
FT   COMPBIAS    860    866       Poly-Arg.
FT   CARBOHYD    219    219       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    271    271       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    285    285       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    322    322       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    372    372       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    394    394       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    400    400       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    407    407       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    414    414       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    478    478       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     36    292       {ECO:0000250}.
FT   DISULFID     83    334       {ECO:0000250}.
FT   DISULFID    165    170       {ECO:0000250}.
FT   VAR_SEQ     839    980       VSVCQEMLQELRHAVSCRKTSRSRRRRRPGGPSRALLSLRA
FT                                VREMRLSNGKLYSAGAGGDAGSAHGGPQRLLDDPGPPSGAR
FT                                PAAPTPCTHVRVCQECRRIQALRASGAGAPPRGLGVPAEAT
FT                                SPPRPRPGPAGPRELAEHE -> TPALHPAACQCSALGPRT
FT                                PLKEPSMLLVKVPSTRVQVAFSRTSLRQVCPFLLQHQLSSL
FT                                YWIQATNVQICCHFSSLKPSPDLTFPPSHRPLSSLLFTALA
FT                                AVGGLPDASSFFFPPISSCPPLQSGIGPCHSTEATLVTSNF
FT                                HV (in isoform 2). {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_035585.
FT   VARIANT     527    527       V -> M (in dbSNP:rs2230298).
FT                                /FTId=VAR_047000.
FT   CONFLICT    436    436       A -> G (in Ref. 1; AAB22591).
FT                                {ECO:0000305}.
FT   CONFLICT    459    461       RFR -> PFP (in Ref. 1; AAB22591).
FT                                {ECO:0000305}.
FT   CONFLICT    711    711       R -> A (in Ref. 1; AAB22591).
FT                                {ECO:0000305}.
SQ   SEQUENCE   980 AA;  109265 MW;  72466FFF64079388 CRC64;
     MPAELLLLLI VAFASPSCQV LSSLRMAAIL DDQTVCGRGE RLALALAREQ INGIIEVPAK
     ARVEVDIFEL QRDSQYETTD TMCQILPKGV VSVLGPSSSP ASASTVSHIC GEKEIPHIKV
     GPEETPRLQY LRFASVSLYP SNEDVSLAVS RILKSFNYPS ASLICAKAEC LLRLEELVRG
     FLISKETLSV RMLDDSRDPT PLLKEIRDDK VSTIIIDANA SISHLILRKA SELGMTSAFY
     KYILTTMDFP ILHLDGIVED SSNILGFSMF NTSHPFYPEF VRSLNMSWRE NCEASTYLGP
     ALSAALMFDA VHVVVSAVRE LNRSQEIGVK PLACTSANIW PHGTSLMNYL RMVEYDGLTG
     RVEFNSKGQR TNYTLRILEK SRQGHREIGV WYSNRTLAMN ATTLDINLSQ TLANKTLVVT
     TILENPYVMR RPNFQALSGN ERFEGFCVDM LRELAELLRF RYRLRLVEDG LYGAPEPNGS
     WTGMVGELIN RKADLAVAAF TITAEREKVI DFSKPFMTLG ISILYRVHMG RKPGYFSFLD
     PFSPAVWLFM LLAYLAVSCV LFLAARLSPY EWYNPHPCLR ARPHILENQY TLGNSLWFPV
     GGFMQQGSEI MPRALSTRCV SGVWWAFTLI IISSYTANLA AFLTVQRMEV PVESADDLAD
     QTNIEYGTIH AGSTMTFFQN SRYQTYQRMW NYMQSKQPSV FVKSTEEGIA RVLNSRYAFL
     LESTMNEYHR RLNCNLTQIG GLLDTKGYGI GMPLGSPFRD EITLAILQLQ ENNRLEILKR
     KWWEGGRCPK EEDHRAKGLG MENIGGIFIV LICGLIIAVF VAVMEFIWST RRSAESEEVS
     VCQEMLQELR HAVSCRKTSR SRRRRRPGGP SRALLSLRAV REMRLSNGKL YSAGAGGDAG
     SAHGGPQRLL DDPGPPSGAR PAAPTPCTHV RVCQECRRIQ ALRASGAGAP PRGLGVPAEA
     TSPPRPRPGP AGPRELAEHE
//